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Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase
Author(s) -
Tsuchiya Kiichiro,
Kawano Youhei,
Kojima Toshiyuki,
Nagata Kisaburo,
Takao Toshifumi,
Okada Masato,
Shinohara Hisaaki,
Maki Kazushige,
Toyama-Sorimachi Noriko,
Miyasaka Nobuyuki,
Watanabe Mamoru,
Karasuyama Hajime
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00127-3
Subject(s) - tyrosine , phosphorylation , tyrosine kinase , gene isoform , biochemistry , microbiology and biotechnology , biology , tyrosine phosphorylation , amino acid , gel electrophoresis , sh2 domain , kinase , chemistry , signal transduction , gene
We have molecularly cloned TPP36, a novel 36 kDa protein with 281 amino acids that was identified as a protein phosphorylated in B progenitor cells following stimulation with pervanadate/H 2 O 2 . Analysis with anti‐TPP36 antiserum revealed that TPP36 was expressed ubiquitously and had an isoform with 236 amino acids, designated TPP32. TPP36/32 were localized mainly in cytoplasm despite the presence of a typical nuclear localization signal sequence. These proteins were phosphorylated preferentially by Abl among a panel of tyrosine kinases examined. Phosphorylation of tyrosine 120 in TPP36/32 led to an apparent mobility shift in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, suggesting conformational change in the phosphorylated protein. Thus, TPP36/32 appear to be novel substrates of Abl tyrosine kinase.